Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.5.5 (CPS)
 1,262 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The half-life of mitochondrial adenosine triphosphatase and the relative rate constants of protein degradation for several fractions of rat liver have been measured by the double-isotope technique. It has been shown that the apparent turnover rates of some mitochondrial enzymes, far apart in size, such as carbamoyl phosphate synthetase, glutamate dehydrogenase and malate dehydrogenase, are not related to molecular weight or to size of subunits. In view of the possibility that mitochondrial proteins are degraded by different mechanisms, it was of interest to determine the half-life of a protein tightly bound to the inner membrane such as adenosine triphosphatase. The rate constants of degradation for rats fed a basal diet and injected at three-day intervals with isotopic leucine were: homogenate, kd = 0.195 days-1; mitochondria, kd = 0.135 days-1; cytosol, kd = 0.140 days-1; microsomes, kd = 0.28 days-1; ATPase, kd = 0.275 days-1. The rate constants of the cellular fractions of liver of rats fed a high protein diet did not change or showed a small increase, compared with those of animals fed the basal diet, while those from rats on the protein-free diet showed a decrease. The rate constant for adenosine triphosphatase showed an increase with high-protein and a decrease with protein-free diet. A procedure for the purification of ATPase from a single liver of a rat is described.
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PMID:Turnover of adenosine triphosphatase from rat liver mitochondria. Effect of high-protein and low-protein diets. 621 5

Coxiella burnetii, an obligate intracellular Gram-negative bacterium, is the etiological agent of Q fever. This work takes advantage of a hypersensitive Escherichia coli genetic system to identify genes involved in resistance to nitrosative stress imposed by reactive nitrogen intermediates. Among the ten candidate genes identified, the transposase, UvrB and DNA topoisomerase IV are involved in DNA transaction; the sigma-32 factor and the putative DNA-binding protein may be involved in transcriptional regulation; IF-2 is involved in protein translation; malate dehydrogenase and carbamoyl-phosphate synthase are metabolic enzymes; and the ABC transporter is a membrane-bound protein. In addition, a hypothetical protein was identified. The role of the DNA repair gene uvrB in resistance to RNI was further confirmed by investigating the sensitivity of uvrB deletion mutant and complementation by C. burnetii uvrB. Deletion of two other components of the UvrABC nuclease, uvrA and uvrC also renders the cell sensitive to RNI. The relationship between UvrABC and nitrosative stress is discussed.
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PMID:Screening of nitrosative stress resistance genes in Coxiella burnetii: Involvement of nucleotide excision repair. 2070 29